Process for removal of excess dye from printed or dyed fabric or yarn

ABSTRACT

The present invention provides a process for removal of excess dye from newly manufactured printed or dyed fabric or yarn, comprising treatment with a rinse liquor comprising at least one enzyme selected from the group consisting of enzymes exhibiting peroxidase activity or laccase activity, an oxidation agent, and at least one mediator selected from the group consisting of aliphatic, cyclo-aliphatic, heterocyclic or aromatic compounds containing the moiety &gt;N—OH, in particular 1-hydroxybenzotriazole.

CROSS-REFERENCE TO RELATED APPLICATIONS

This application is a continuation of application Ser. No. 09/221,653,filed Dec. 23, 1998 now U.S. Pat. No. 6,048,367, and claims priorityunder 35 U.S.C. 119 of Danish application 1526/97 filed Dec. 23, 1997,and of U.S. provisional application No. 60/071,184 filed Jan. 12, 1998,the contents of which are fully incorporated herein by reference.

The present invention relates to a novel method of removing excess dyefrom newly printed or dyed fabric or yarn as well as a system and acomposition for use in the method.

BACKGROUND OF THE INVENTION

Printing and dyeing of textiles is carried out by applying dyes to thetextile by any appropriate method for binding the dyestuff to the fibresin the textiles. Excess soluble dyestuff not bound to the fibres must beremoved after dyeing to ensure fastness of the dyed textiles and toprevent unwanted dye transfer during laundering of the textiles by theconsumer.

Generally, a large amount of water is required for complete removal ofexcess dye. In a conventional process the printed or dyed textile isfirst rinsed with cold water, then washed at high temperature with theaddition of a suitable additive to decrease back-staining, likepoly(vinylpyrrolidone) (PVP). The process is repeated until asatisfactory amount of dyestuff (and thickeners) has been removed. PVPcan be added to reduce back-staining during rinsing, but this compounddoes not bleach the dye and is relatively expensive. Furthermore, thewaste liquor from a conventional process tends to be strongly colouredand may represent a disposal problem, which is not reduced by the use ofPVP.

WO 92/18687 discloses a method of bleaching excess dye from printed ordyed fabric by treating with a liquor containing an enzyme exhibitingperoxidase activity or oxidase activity, an O₂ or H₂O₂ source asapplicable, and optionally an additional oxidizable substrate, such as ametal ion, a halide ion or an organic compound, such as a phenol.

However, the concentrations of such additional substrates necessary forenzymatically bleaching the excess dye in the rinse liquor may present arisk of bleaching the dyed textiles themselves.

Accordingly, it is an object of the present invention to provide amethod for removing or bleaching excess dye without bleaching the dyedtextile. This is achieved by a process for removal of excess dye fromnewly manufactured printed or dyed fabric or yarn comprising treatmentwith a rinse liquor comprising

at least one enzyme selected from the group consisting of enzymesexhibiting peroxidase activity or laccase activity,

an oxidation agent, and

at least one mediator selected from the group consisting of aliphatic,cyclo-aliphatic, heterocyclic or aromatic compounds containing themoiety >N—OH, and

optionally additives.

In the present invention the term “mediator” means an additionaloxidizable substance improving the bleaching performance.

By suitable combination of mediator and enzyme it is possible to avoidbleaching of the dyed textile while bleaching dyes in solution, therebyreducing the amount of unbleached dye deposited on the fibres and thusincreasing the wet fastness of the dyed or printed textile.

By this process it is furthermore possible to reduce the number ofrinsing steps and the temperature of the rinsing water in the rinsingsteps compared to the conventional processes, thereby saving energy andcosts.

Another object of the present invention is a system for removal ofexcess dye from newly manufactured printed or dyed fabric or yarn, whichis a multi-component system comprising at least one enzyme selected fromthe group consisting of enzymes exhibiting peroxidase activity orlaccase activity, an oxidation agent, and at least one mediator selectedfrom the group consisting of aliphatic, cyclo-aliphatic, heterocyclic oraromatic compounds containing the moiety >N—OH, and optionallyadditives, such as rinsing additives.

The components of the system may be combined as a solution, a slurry orgranulates depending on the specific enzymes and mediators selected.

A further object of the present invention is the use of the componentsspecified above for the preparation of a multi-component system forremoval of excess dye or print from newly manufactured fabric or yarn.

DETAILED DESCRIPTION OF THE INVENTION

Fabric or Yarn

The process of the invention is applicable to all types of textilematerials, both natural fibres and synthetic fibres as well as blendsthereof. Typical examples are cellulosic fibres (cotton and flax),modified cellulose fibres (e.g. acetate and triacetate), protein fibres(e.g. wool and silk), polyamide fibres (e.g. nylon 6 and 6,6), polyesterfibres (e.g. poly(ethylene terephthalate)) and acrylic fibres.

The process of the invention may be applied to dyed yarn, to knitted,woven or non-woven fabric, or to garments made from dyed and/or printedfabric, especially garments made from differently coloured material.

Printing Method

The process of the invention is suited for excess dye bleaching afterany kind of textile printing. Examples of commonly used techniques areprinting on a Rotation film, a Rouleaux, a Flash film, or a Transferfilm device. After printing the dye is fixed on the textile by e.g.steaming or treatment with hot air.

Dyeing Method

The process of the invention is suited for excess dye bleaching afterany kind of dyeing. The dyeing of textiles is for example carried out bypassing the fabric through a concentrated solution of dye, followed bystorage of the wet fabric in a vapour tight enclosure to permit time fordiffusion and reaction of the dye with the fabric substrate prior torinsing off un-reacted dye. Alternatively, the dye may be fixed bysubsequent steaming of the textile prior to rinsing.

The process applies to any kind of dyes, such as reactive dyes.

Enzyme

Enzymes exhibiting peroxidase activity or laccase activity are thosewhich by using hydrogen peroxide or molecular oxygen, respectively arecapable of oxidising a variety of compounds, such as phenols andaromatic amines.

According to the invention the concentration of enzyme is 0.005 to 5 mgenzyme protein per 1 of rinse liquor, preferably, 0.02 to 2 mg enzymeprotein per 1 of rinse liquor, more preferably 0.05 to 1 mg enzymeprotein per 1 of rinse liquor. According to the liquor ratio, this maybe translated to dosages of enzyme per kg of fabric, e.g. at a liquorratio of 10:1, the most preferred enzyme dosage is from 0.5 to 10 mgenzyme per kg of textile fabric.

Peroxidase Activity Exhibiting Enzymes

An enzyme exhibiting peroxidase activity may be any peroxidase comprisedby the enzyme classification (EC 1.11.1.7), or a haloperoxidase, such asa chloride peroxidase (EC 1.11.1.10) or any fragment or synthetic orsemisynthetic derivatives thereof exhibiting enzymatic activity (e.g.porphyrin ring systems or microperoxidases, cf. e.g. U.S. Pat. No.4,077,768, EP 537 381, WO 91/05858 and WO 92/16634). Such enzymes areknown from microbial, plant and animal origins.

Preferably, the peroxidase employed in the method of the invention isproducible by plants (e.g. horseradish or soybean peroxidase), inparticular soybean peroxidase, or by microorganisms, such as fungi(including filamentous fungi and yeasts) or bacteria.

Some preferred fungi include strains belonging to the subdivisionDeuteromycotina, class Hyphomycetes, e.g., Fusarium, Humicola,Tricoderma, Myrothecium, Verticillum, Arthromyces, Caldariomyces,Ulocladium, Embellisia, Cladosporium or Dreschlera, in particularFusarium oxysporum (DSM 2672), Humicola insolens, Trichoderma resii,Myrothecium verrucana (IFO 6113), Verticillum alboatrum, Verticillumdahlie, Arthromyces ramosus (FERM P-7754), Caldariomyces fumago,Ulocladium chartarum, Embellisia alli or Dreschlera halodes.

Other preferred fungi include strains belonging to the subdivisionBasidiomycotina, class Basidiomycetes, e.g. Coprinus, Phanerochaete,Coriolus or Trametes, in particular Coprinus cinereus f. microsporus(IFO 8371), Coprinus macrorhizus, Phanerochaete chrysosporium (e.g.NA-12) or Trametes (some classes previously called Polyporus have beenrenamed to Trametes), e.g., T. versicolor (e.g. PR4 28-A).

Further preferred fungi include strains belonging to the subdivisionZygomycotina, class Mycoraceae, e.g. Rhizopus or Mucor, in particularMucor hiemalis.

Some preferred bacteria include strains of the order Actinomycetales,e.g., Streptomyces spheroides (ATTC 23965), Streptomyces thermoviolaceus(IFO 12382) or Streptoverticillum verticillium ssp. verticillium.

Other preferred bacteria include Bacillus pumilus (ATCC 12905), Bacillusstearothermophilus, Rhodobacter sphaeroides, Rhodomonas palustri,Streptococcus lactis, Pseudomonas purrocinia (ATCC 15958) or Pseudomonasfluorescens (NRRL B-11).

Further preferred bacteria include strains belonging to Myxococcus,e.g., M. virescens.

The peroxidase may furthermore be one which is producible by a methodcomprising cultivating a host cell transformed with a recombinant DNAvector which carries a DNA sequence encoding said peroxidase as well asDNA sequences encoding functions permitting the expression of the DNAsequence encoding the peroxidase, in a culture medium under conditionspermitting the expression of the peroxidase, and recovering theperoxidase from the culture.

Particularly, a recombinantly produced peroxidase is a peroxidasederived from a Coprinus sp., in particular C. macrorhizus or C. cinereusaccording to WO 92/16634, or a variant thereof.

In the context of this invention, peroxidase acting compounds compriseperoxidase active fragments derived from cytochromes, hemoglobin orperoxidase enzymes, and synthetic or semisynthetic derivatives thereof,e.g. iron complexes of porphyrin or phthalocyanine and derivativesthereof.

Laccase and Laccase Related Enzymes

In the context of this invention, the term “enzymes exhibiting laccaseactivity” means laccases and laccase related enzymes, such as anylaccase comprised by the enzyme classification (EC 1.10.3.2), anycatechol oxidase comprised by the enzyme classification (EC 1.10.3.1),any bilirubin oxidase comprised by the enzyme classification (EC1.3.3.5) or any monophenol monooxygenase comprised by the enzymeclassification (EC 1.14.99.1).

The laccases are known from microbial and plant origin. The microbiallaccases may be derived from bacteria or fungi (including filamentousfungi and yeasts) and suitable examples include a laccase derivable froma strain of Aspergillus, Neurospora, e.g., N. crassa, Podospora,Botrytis, Collybia, Fomes, Lentinus, Pleurotus, Trametes, e.g., T.villosa and T. versicolor, Rhizoctonia, e.g., R. solani, Coprinus, e.g.C. plicatilis and C. cinereus, Psatyrella, Myceliophthora, e.g. M.thermophila, Schytalidium, Polyporus, e.g., P. pinsitus, Phlebia, e.g.,P. radiata (WO 92/01046), or Coriolus, e.g., C. hirsutus (JP 2-238885),in particular a laccase derivable from a strain of Fomes, Trametes,Rhizoctonia, Coprinus, Myceliophthora, Schytalidium, or Polyporus.

The laccase or the laccase related enzyme may furthermore be one whichis producible by a method comprising cultivating a host cell transformedwith a recombinant DNA vector which carries a DNA sequence encoding saidlaccase as well as DNA sequences encoding functions permitting theexpression of the DNA sequence encoding the laccase, in a culture mediumunder conditions permitting the expression of the laccase, andrecovering the laccase from the culture.

Oxidation Agent

If the oxidizing enzyme requires a source of hydrogen peroxide, thesource may be hydrogen peroxide or a hydrogen peroxide precursor for insitu production of hydrogen peroxide, e.g., a percarbonate or aperborate, a persulfate, such as a trioxo(peroxo)sulfate or aμ-peroxo-bis(trioxosulfate), a hydrogen peroxide-urea addition compound,a peroxycarboxylic acid or a salt thereof or a hydrogen peroxidegenerating enzyme system, e.g., an oxidase and a substrate for theoxidase, e.g. an amino acid oxidase and a suitable amino acid.

Hydrogen peroxide may be added at the beginning of or during theprocess, e.g., in a concentration corresponding to 0.01-50 mM H₂O₂,preferably 0.1 to 5 mM.

If the oxidizing enzyme requires molecular oxygen, molecular oxygen fromthe atmosphere will usually be present in sufficient quantity. Otherwisepure O₂ may be led to the rinse liquor, or an O₂ generating enzymaticsystem, e.g. a system based on hydrogen peroxide and a catalase, may beadded.

Mediator

According to the invention at least one mediator selected from the groupconsisting of aliphatic, cyclo-aliphatic, heterocyclic or aromaticcompounds containing the moiety >N—OH is added to the rinse liquor. In apreferred embodiment of the invention the

mediator is a compound of the general formula I:

wherein

R¹, R², R³, R⁴ are individually selected from the group consisting ofhydrogen, halogen, hydroxy, formyl, carboxy and salts and estersthereof, amino, nitro, C₁-C₁₂ alkyl, C₁-C₆ alkoxy, carbonyl(C₁-C₁₂alkyl), aryl, in particular phenyl, sulfo, aminosulfonyl, carbamoyl,phosphono, phosphonooxy, and salts and esters thereof, wherein the R¹,R², R³, R⁴ may be substituted with R⁵, wherein R⁵ represents hydrogen,halogen, hydroxy, formyl, carboxy and salts and esters thereof, amino,nitro, C₁-C₁₂ alkyl, C₁-C₆ alkoxy, carbonyl(C₁-C₁₂ alkyl), aryl, inparticular phenyl, sulfo, aminosulfonyl, carbamoyl, phosphono,phosphonooxy, and salts and esters thereof,

[X] represents a group from (—N═N—), (—N═CR⁶—)_(m), (—CR⁶═N—)_(m),(—CR⁷═CR⁸—)_(m),

and m is 1 or 2.

In a more preferred embodiment of the invention the mediator is acompound of the general formula II:

wherein R¹, R², R³, R⁴ are individually selected from the groupconsisting of hydrogen, halogen, hydroxy, formyl, carboxy and salts andesters thereof, amino, nitro, C₁-C₁₂ alkyl, C₁-C₆ alkoxy,carbonyl(C₁-C₁₂ alkyl), aryl, in particular phenyl, sulfo,aminosulfonyl, carbamoyl, phosphono, phosphonooxy, and salts and estersthereof, wherein the R¹, R², R³, R⁴ may be substituted with R⁵, whereinR⁵ represents hydrogen, halogen, hydroxy, formyl, carboxy and salts andesters thereof, amino, nitro, C₁-C₁₂ alkyl, C_(l)-C₆ alkoxy,carbonyl(C₁-C₁₂ alkyl), aryl, in particular phenyl, sulfo,aminosulfonyl, carbamoyl, phosphono, phosphonooxy, and salts and estersthereof.

The mediator may also be a salt or an ester of formula I or II.

Further preferred mediators are oxoderivatives and N-hydroxy derivativesof heterocyclic compounds and oximes of oxo- and formyl-derivatives ofheterocyclic compounds, said heterocyclic compounds includingfive-membered nitrogen-containing heterocycles, in particular pyrrol,pyrazole and imidazole and their hydrogenated counterparts (e.g.pyrrolidine) as well as triazoles, such as 1,2,4-triazole; six-memberednitrogen-containing heterocycles, in particular mono-, di- andtriazinanes (such as piperidine and piperazine), morpholine and theirunsaturated counterparts (e.g. pyridine and pyrimidine); and condensedheterocycles containing the above heterocycles as substructures, e.g.indole, benzothiazole, quinoline and benzoazepine.

Examples of preferred mediators from these classes of compounds arepyridine aldoximes; N-hydroxypyrrolidinediones such asN-hydroxysuccinimide and N-hydroxyphthalimide;3,4-dihydro-3-hydroxybenzo[1,2,3]triazine-4-one; formaldoxime trimer(N,N′,N″-trihydroxy-1,3,5-triazinane); and violuric acid(1,3-diazinane-2,4,5,6-tetrone-5-oxime).

Still further mediators which may be applied in the invention includeoximes of oxo- and formyl-derivatives of aromatic compounds, such asbenzoquinone dioxime and salicylaldoxime (2-hydroxybenzaldehyde oxime),and N-hydroxyamides and N-hydroxyanilides, such as N-hydroxyacetanilide.

Preferred mediators are selected from the group consisting of1-hydroxybenzotriazole; 1-hydroxybenzotriazole hydrate;1-hydroxybenzotriazole sodium salt; 1-hydroxybenzotriazole potassiumsalt; 1-hydroxybenzotriazole lithium salt; 1-hydroxybenzotriazoleammonium salt; 1-hydroxybenzotriazole calcium salt;1-hydroxybenzotriazole magnesium salt; and1-hydroxybenzotriazole-6-sulphonic acid.

A particularly preferred mediator is 1-hydroxybenzotriazole.

All the specifications of N-hydroxy compounds above are understood toinclude tautomeric forms such as N-oxides whenever relevant.

Usually, the concentration of mediator in the rinse liquor is from 0.1μM to 50 mM, preferably 1 μM to 1 mM, more preferably 10 μM to 0.5 mM.

Additives

The rinse liquor may comprise further additives, such as surfactantsand/or water conditioning agents.

Multi-component System

In order to carry out the process described above a multi-componentsystem is added to the rinse liquor in at least one of the rinsingsteps.

The components of the multi-component system may individually be in oneof several product forms, such as a slurry, a solution or a granulate.

In one embodiment of the invention two components are mixed in therepresented form, such as a co-granulate, a solution or a slurrycomprising enzyme and mediator.

In cases of co-granulates, the co-granulate may comprise at least oneenzyme and at least one mediator. Another example of a co-granulate is agranulate comprising at least two different enzymes and optionally atleast one mediator.

In a further embodiment the system is a mixture of granulates whereinthe component(s) in one granulate is (are) enzyme(s) and thecomponent(s) in another granulate is (are) mediator(s).

According to the present invention a preferred multi-component systemcomprises at least one enzyme selected from the group consisting ofenzymes exhibiting peroxidase activity or laccase activity, optionallyan oxidation agent, and at least one mediator selected from the groupconsisting of aliphatic, cyclo-aliphatic, heterocyclic or aromaticcompounds containing the moiety >N—OH as described above, and optionallyadditives, such as rinsing additives.

The enzymes exhibiting peroxidase activity or laccase activity arepreferably as described above.

The system may comprise an oxidation agent, but in cases where theenzyme is an enzyme exhibiting laccase activity, molecular oxygen fromthe atmosphere is normally sufficient, and the system used will notcomprise an oxidation agent. However, when the enzymes used requireaddition of an oxidation agent those are as described above. In allcases wherein a H₂O₂ source is the oxidation agent the enzyme andoxidation agent may not be mixed before use.

The mediator is as described above, in a preferred embodiment themediator is selected from the group consisting of oxoderivatives andN-hydroxy derivatives of heterocyclic compounds and oximes of oxo- andformyl-derivatives of heterocyclic compounds, said heterocycliccompounds including five-membered nitrogen-containing heterocycles, inparticular pyrrol, pyrazole and imidazole and their hydrogenatedcounterparts (e.g. pyrrolidine) as well as triazoles, such as1,2,4-triazole; six-membered nitrogen-containing heterocycles, inparticular mono-, di- and triazinanes (such as piperidine andpiperazine), morpholine and their unsaturated counterparts (e.g.pyridine and pyrimidine); and condensed heterocycles containing theabove heterocycles as substructures, e.g. indole, benzothiazole,quinoline and benzoazepine.

Examples of preferred mediators from these classes of compounds arepyridine aldoximes; N-hydroxypyrrolidinediones such asN-hydroxysuccinimide and N-hydroxyphthalimide;3,4-dihydro-3-hydroxybenzo[1,2,3]triazine-4-one; formaldoxime trimer(N,N′,N″-trihydroxy-1,3,5-triazinane); and violuric acid(1,3-diazinane-2,4,5,6-tetrone-5-oxime).

Still further mediators which may be applied in the invention includeoximes of oxo- and formyl-derivatives of aromatic compounds, such asbenzoquinone dioxime and salicylaldoxime (2-hydroxybenzaldehyde oxime),and N-hydroxyamides and N-hydroxyanilides, such as N-hydroxyacetanilide.

A particularly preferred mediator is 1-hydroxybenzotriazole.

All the specifications of N-hydroxy compounds above are understood toinclude tautomeric forms such as N-oxides whenever relevant.

A further aspect of the present invention is the use of componentscomprising

at least one enzyme selected from the group consisting of enzymesexhibiting peroxidase activity or laccase activity,

optionally an oxidation agent, and

at least one mediator selected from the group consisting of aliphatic,cyclo-aliphatic, heterocyclic or aromatic compounds containing themoiety >N—OH, and

optionally additives

for the preparation of a multi-component system for removal of excessdye or print from newly manufactured fabric or yarn.

Process Conditions

The removal of excess dye, according to the invention, may compriserinsing with rinse liquor in 2 to 6 rinsing steps, more preferred in 2to 5 rinsing steps, even more preferred in 2 to 4 rinsing steps, inparticular in 3 to 4 rinsing steps. The amount of rinsing steps isdependent on the concentration of the mediator and of the concentrationof the peroxidase.

The multi-component system as defined according to this invention may beused in any of the rinsing steps performed, however it is preferablyadded in one of the last rinsing steps, in particular in the third orfourth rinsing step.

The process may be run in batch mode or continuous mode. The process maybe applied on a winch, a beck, a jet dyer, an open-width washingmachine, a J or U box, a steamer, or any other equipment availablesuitable for a rinsing process.

The process conditions must be chosen according to the characteristicsof the enzyme in question. The temperature at the rinsing stepcomprising a multi-component system as defined above is preferablyranging from 40° C. to 80° C., such as from 50° C. to 70° C., and pH istypically in the range of 5.5-9.5, such as 6.5-9.

Fastness

Fastness (wet, crock, light, etc.) may be measured by various methods asknown in the art. Wet fastness may be measured as described below.Colourfastness to crocking, which is designed to determine the amount ofcolour transferred from the surface of coloured materials to othersurfaces by rubbing, may be measured according to AATCC Test Method8-1996. Colourfastness to light, in which samples of the material to betested and the agreed upon comparison standard(s) are exposedsimultaneously to a light source under specified conditions, may bemeasured according to AATCC Test Method 16-1993.

Wet Fastness

The multi-component system as defined above is added to the rinsingliquor to prevent re-deposition of solubilised excess dye by bleachingit in solution.

The wet fastness or water fastness reflects the degree to which this hassuccessfully been achieved.

In the present invention the wet fastness is measured by the standardmethod (DIN 54 006). Briefly, the method comprises soaking a dyed fabricand pressing it together with swatches of white fabric. After separatedrying of the fabrics, the swatches are evaluated for staining.

The degree of wet fastness is indicated on a scale, the higher numberthe better wet fastness. 1 means very low wet fastness, whereas 5 meansvery high wet fastness.

Colour Measurement (Example 5)

A Gretag-Mecbath Colour Eye 3100 was used according to themanufacturer's instructions to evaluate the chromaticity using thechange in the colour space coordinates L*a*b* (CIELAB-system), where asusual:

L* gives the change in white/black on a scale from 0 to 100, and adecrease in L* means an increase in black colour (decrease in whitecolour) and an increase in L* means an increase in white colour(decrease in black colour).

a* gives the change in red/green, and a decrease in a* means an increasein green colour (decrease in red colour), and an increase in a* means anincrease in red colour (decrease in green colour).

b* gives the change in blue/yellow, and a decrease in b* means anincrease in blue colour (decrease in yellow colour), and an increase inb* means an increase in yellow colour (decrease in blue colour) (Vide WO96/12846 NOVO).

The Gretag-Macbeth Colour Eye 3100 was operated in the L*a*b* colourspace. The light source was D65 standard light. The software used forevaluation was Optiview Quality Control 1.7c. The observation angle was10°. The instrument was calibrated using a Macbeth calibration plate(white). Each result was an average of 10 measurements. Fabric rinsedwithout enzyme and mediator was measured and the coordinates L*a*b* werecalculated and entered as a reference. The coordinates of the sampleswere then for each of L*, a*, b* calculated as the difference (Δ) of theaverage of the measurements on each swatch from the reference value.

The present invention is further illustrated in the following exampleswhich are not in any way intended to limit the scope of the invention asclaimed.

EXAMPLE 1

Reactive Dyeing of Cotton Fabric Followed by an Enzymatic RinsingProcess

Knitted, bleached 100% cotton was dyed in a Mathis jet-dyer (laboratoryscale jet dyeing machine) under the following conditions:

Water: softened water, 10 l/kg of fabric

Temperature: 50° C.

Dyestuff: 4% LEVAFIX Scarlet E-2GA (Reactive Red 123)

Na₂SO₄: 50 g/l

Na₂CO₃: 4 g/l

NaOH (32%): 2 ml/l

LEVEGAL RL: 1.0 g/l (levelling agent)

ERKANTOL NR: 1.0 g/l (wetting agent)

PERSOFTAL L: 1.0 g/l (crease-preventing agent)

RESPUMIT S: 1.0 g/l (antifoaming agent)

LEVAFIX Scarlett E-2GA is a product of DyStar.

LEVEGAL RL, ERKANTOL NR, PERSOFTAL L and RESPUMIT S are products ofBAYER.

The dyeing process started at 50° C. by addition of dyestuff, Na₂SO₄,LEVEGAL RL, ERKANTOL NR, PERSOFTAL L and RESPUMIT S.

Na₂CO₃ was added 30 minutes after start and NaOH 60 minutes after start.During the whole process the temperature was held at 50° C.

60 minutes after addition of NaOH the dyeing process was stopped bydraining off the dyeing liquor, whereafter the rinsing process wasstarted.

The rinsing process was carried out as follows:

First Rinsing Step

Addition of fresh softened water; 10 l/kg fabric.

Rinsing 10 minutes at 40° C.

Draining the rinsing liquor.

Second Rinsing Step

Addition of fresh softened water; 10 l/kg fabric.

Addition of 10 ml/l of acetic acid (6% solution in water)

Rinsing 20 minutes at 95° C.

Draining the rinsing liquor.

Third Rinsing Step

Addition of fresh softened water; 10 l/kg fabric.

Addition of 5.0 ml/l of potassium phosphate buffer (1.0 M, pH=7.0)

Rinsing 40 minutes at 60° C.

Addition of 0.8 mg/l Peroxidase SP502, 55 mg/l (0.4 mM) HOBT and 39 mg/l(0.4 mM) H₂O₂ (35% solution in water)

Rinsing 10 minutes at 60° C.

Draining the rinsing liquor.

SP502 was a liquid preparation of recombinant Coprinus cinereusperoxidase supplied by Novo Nordisk A/S (produced as described in WO92/16634). HOBT was 1-hydroxybenzotriazole ex Sigma.

The fabric was squeezed and dried. The wet fastness was determinedaccording to DIN 54 006. The degree of fastness was found to be 3(adjacent fabric cotton).

EXAMPLE 2

(For Comparison)

Conventional 3 Step Rinsing Process

The dyeing process was carried out as described in Example 1. Therinsing steps were carried out as follows.

First Rinsing Step

Addition of fresh softened water; 10 l/kg fabric.

Rinsing 10 minutes at 40° C.

Draining the rinsing liquor.

Second Rinsing Step

Addition of fresh softened water; 10 l/kg fabric.

Rinsing 20 minutes at 95° C.

Draining the rinsing liquor.

Third Rinsing Step

Addition of fresh softened water; 10 l/kg fabric.

Rinsing 10 minutes at 80° C.

Draining the rinsing liquor.

The fabric was squeezed and dried. The wet fastness was determinedaccording to DIN 54 006. The degree of fastness was found to be 2(adjacent fabric cotton)

EXAMPLE 3

(For Comparison)

Conventional 4 Step Rinsing Process

The dyeing process was carried out as described in Example 1. Therinsing steps were carried out as follows.

First Rinsing Step

Addition of fresh softened water; 10 l/kg fabric.

Rinsing 10 minutes at 40° C.

Draining the rinsing liquor.

Second Rinsing Step

Addition of fresh softened water; 10 l/kg fabric.

Rinsing 10 minutes at 70° C.

Draining the rinsing liquor.

Third Rinsing Step

Addition of fresh softened water; 10 l/kg fabric.

Rinsing 20 minutes at 95° C.

Draining the rinsing liquor.

Fourth Rinsing Step

Addition of fresh softened water; 10 l/kg fabric.

Rinsing 10 minutes at 40° C.

Draining the rinsing liquor.

The fabric was squeezed and dried. The wet fastness was determinedaccording to DIN 54 006. The degree of fastness was found to be 2-3(adjacent fabric cotton).

EXAMPLE 4

(For Comparison)

Conventional 6 Step Rinsing Process

The dyeing process was carried out as described in Example 1. Therinsing steps were carried out as follows.

First Rinsing Step

Addition of fresh softened water; 10 l/kg fabric.

Rinsing 10 minutes at 40° C.

Draining the rinsing liquor.

Second Rinsing Step

Addition of fresh softened water; 10 l/kg fabric.

Rinsing 10 minutes at 70° C.

Draining the rinsing liquor.

Third Rinsing Step

Addition of fresh softened water; 10 l/kg fabric.

Rinsing 10 minutes at 70° C.

Draining the rinsing liquor.

Fourth Rinsing Step

Addition of fresh softened water; 10 l/kg fabric.

Rinsing 20 minutes at 95° C.

Draining the rinsing liquor.

Fifth Rinsing Step

Addition of fresh softened water; 10 l/kg fabric.

Rinsing 10 minutes at 70° C.

Draining the rinsing liquor.

Sixth Rinsing Step

Addition of fresh softened water; 10 l/kg fabric.

Rinsing 10 minutes at 40° C.

Draining the rinsing liquor.

The fabric was squeezed and dried. The wet fastness was determinedaccording to DIN 54006. The degree of fastness was found to be 3(adjacent fabric cotton).

Conclusion: The wet fastness 3 (corresponding to the conventional 6 steprinsing process) was also obtained by the process according to theinvention (see Example 1), whereby a substantial amount of rinsing stepscan be avoided (saving water and energy and process time).

EXAMPLE 5

Reactive Dyeing of Cotton Fabric Followed by Enzymatic Rinsing ProcessesUsing Two Different Mediators

Knitted, bleached 100% cotton was dyed in a Mathis jet-dyer (laboratoryscale jet dyeing machine) at the following conditions:

Water: softened water, 10 l/kg of fabric

Dyestuff:

1% Remazol Yellow RR

1% Remazol Red RR

1% Remazol Blue RR

Na₂SO₄: 70 g/l

Na₂CO₃: 5 g/l

NaOH (32% in water): 3 ml/l

LEVEGAL RL: 1.0 g/l (levelling agent)

ERKANTOL NR: 1.0 g/l (wetting agent)

PERSOFTAL L: 1.0 g/l (crease-preventing agent)

Remazol Yellow RR, Remazol Red RR, and Remazol Blue RR are products ofDyStar.

LEVEGAL RL, ERKANTOL NR, and PERSOFTAL L are products of BAYER.

The dyeing process started at 30° C. by addition of Na₂CO₃, NaOH (1ml/l), Na₂SO₄, LEVEGAL RL, ERKANTOL NR, PERSOFTAL L. The dyestuffs wereadded 15 minutes after start. 30 minutes after start the temperature wasincreased up to 50° C. within 20 minutes. 30 minutes after reaching 50°C. the remaining NaOH (2 ml/l) was added. 45 minutes after the additionof NaOH (2 ml/l) the dyeing process was finished by draining off thedyeing liquor, whereafter the rinsing process was started.

The following rinsing process was carried out for each mediator(1-hydroxybenzotriazole (according to the invention); and methylsyringate (comparison)):

First Rinsing Step

Addition of fresh softened water; 10 l/kg fabric.

Rinsing 10 minutes at 40° C.

Draining the rinsing liquor.

Second Rinsing Step

Addition of fresh softened water; 10 l/kg fabric.

Addition of 10 ml/l of acetic acid (6% solution in water)

Rinsing 20 minutes at 95° C.

Draining the rinsing liquor.

Third Rinsing Step

Addition of fresh softened water; 10 l/kg fabric.

Addition of 5.0 ml/l of potassium phosphate buffer (1.0 M, pH=7.0)

Rinsing 40 minutes at 60° C.

Addition of 0.8 mg/l Peroxidase SP502, 0.4 mM mediator and 39 mg/l (0.4mM) H₂0₂ (35% solution in water)

Rinsing 10 minutes at 60° C.

Draining the rinsing liquor.

SP502 was a liquid preparation of recombinant Coprinus cinereusperoxidase supplied by Novo Nordisk A/S.

The fabric was squeezed and dried. A colour measurement was performedusing a colour measuring instrument (Gretag-Macbeth Colour Eye 3100) asdescribed above.

Results

Mediator: 1-hydroxybenzotriazole

ΔL*=0.756

Δa*=0.045

Δb*=0.022

Mediator: Methyl Syringate

ΔL*=3.142

Δa*=0.134

Δb*=0.834

Conclusion: It can be seen that methyl syringate has a significant andundesired influence on the chromaticity of the fabric. The positive Δb*of 0.834 indicates a very strong and not acceptable increase in yellowcolour whereas a Δb* of 0.022 which is found for 1-hydroxybenzotriazoleis negligible and not visible. It is seen that also ΔL* and Δa* aresignificantly smaller in the treatment according to the invention thanin the comparison treatment.

EXAMPLE 6

Enzymatic Bleaching of Soluble Dyes

The dyes tested were Reactive Black 5 (Remazol Black B), Reactive Red198 (Remazol Red RB), Reactive Blue 220(Remazol Brilliant Blue BB),Reactive Blue 21 (Remazol Turquoise Blue G), and Reactive Orange 107(Remazol Golden Yellow RNL), all ex Dystar. All dyes were dissolved in a0.5 mM sodium phosphate buffer (pH 7.0) to an initial absorbance ofapproximately 0.4 at the wavelength λmax of maximum absorbance withinthe visible range. The solutions were then placed in a thermostatedquartz cell in a HP 8453 diode array spectrophotometer, the threecomponents of the enzymatic oxidation system were added (CiP to 0.2mg/l, HOBT to 100 μM, hydrogen peroxide to 200 μM), and the absorbanceABS(λmax) at λmax monitored over time. The degree of bleaching at 5 min,i.e. the decrease in ABS(λmax) over 5 min divided by ABS(λmax) at t=0,is shown below, measured at three temperatures.

Degree of Bleaching at 5 Min(%)

Reactive Black 5 (λmax=596 nm):

79 (60° C.); 82 (70° C.); 72 (80° C.);

Reactive Red 198 (λmax=517 nm):

97 (60° C.); 100 (70° C.); 88 (80° C.);

Reactive Blue 220 (λmax=608 nm):

100 (60° C.); 98 (70° C.); 30 (80° C.);

Reactive Blue 21 (λmax=663 nm):

100 (60° C.); 88 (70° C.); 61 (80° C.);

Reactive Orange 107 (λmax=408 nm):

90 (60° C.); 67 (70° C.); 36 (80° C.).

This example demonstrates that one of the preferred mediators accordingto the invention, HOBT (1-hydroxybenzotriazole), combined with Coprinuscinereus peroxidase (CiP) and hydrogen peroxide, provides high degreesof bleaching of soluble dyes in short time with a range of reactivedyes.

What is claimed is:
 1. A process for removal of excess dye from newlymanufactured printed or dyed fabric or yarn, said process comprising:(a) subjecting said fabric to at least one rinsing step after printingor dyeing using a rinsing liquor that lacks a peroxidase or laccase,oxidation agent, and mediator; and (b) treating said rinsed fabric oryarn with a liquor comprising at least one enzyme selected from thegroup consisting of enzymes exhibiting peroxidase activity and enzymesexhibiting laccase activity, an oxidation agent, at least one mediator,wherein said mediator is a compound of the general formula

wherein R¹, R², R³, R⁴ are individually selected from the groupconsisting of hydrogen, halogen, hydroxy, formyl, carboxy and salts andesters thereof, amino, nitro, C₁-C₁₂ alkyl, C₁-C₆ alkoxy,carbonyl(C₁-C₁₂ alkyl), aryl, sulfo, aminosulfonyl, carbamoyl,phosphono, phosphonooxy, and salts and esters thereof, wherein the R¹,R², R³, R⁴ may be substituted with R⁵, wherein R⁵ represents hydrogen,halogen, hydroxy, formyl, carboxy and salts and esters thereof, amino,nitro, C₁-C₁₂ alkyl, C₁-C₆ alkoxy, carbonyl(C₁-C₁₂ alkyl), aryl, sulfo,aminosulfonyl, carbamoyl, phosphono, phosphonooxy, and salts and estersthereof, and optionally additives.
 2. A process according to claim 1,wherein the enzyme is a laccase (EC 1.10.3.2), a catechol oxidase (EC1.10.3.1), a bilirubin oxidase (EC 1.3.3.5), a peroxidase (EC 1.11.1.7),or a haloperoxidase, or any fragment derived therefrom exhibitingenzymatic activity or synthetic or semisynthetic derivatives thereof. 3.A process according to claim 2, wherein the peroxidase is derived from astrain of Coprinus or from soybean.
 4. A process according to claim 1,wherein the mediator is 1-hydroxybenzotriazole.
 5. A process accordingto claim 1, wherein step (a) comprises at least two rinsing steps.
 6. Aprocess according to claim 1, wherein step (a) comprises at least fiverinsing steps.
 7. A process according to claim 1, wherein said fabric oryarn has been dyed using a dyeing method selected from the groupconsisting of continuous dyeing and batch dyeing.
 8. A process accordingto claim 1, wherein said batch dyeing method is selected from the groupconsisting of pad-batch and pad-steam dyeing.
 9. A process according toclaim 1, wherein said fabric or yarn comprises a fiber selected from thegroup consisting of cellulosic, protein, polyamide, polyester, andacrylic fibers.